Abstract
Hepatitis B virus (HBV) is a major pathogen that causes acute/chronic hepatitis. Continuous HBV infection can lead to the development of hepatocellular carcinoma (HCC). Although several different anti-HBV treatments are available for chronic hepatitis B patients, discontinuing these medications is difficult. Patients with chronic hepatitis B at high risk for HCC therefore require close observation. However, no suitable biomarkers for detecting high-risk groups for HCC exist, except for serum HBV-DNA, but a number of HCC biomarkers are used clinically, such as alpha-fetoprotein (AFP) and protein induced by vitamin K absence-II (PIVKA-II). Glycosylation is an important post-translational protein modification involved in many human pathologic conditions. HBV surface proteins contain various oligosaccharides, and several reports have described their biological functions. Inhibition of HBV glycosylation represents a potential novel anti-HBV therapy. It is thought that glycosylation of hepatocytes/hepatoma cells is also important for HBV infection, as it prevents HBV from infecting cells other than hepatocytes, even if the cells express the HBV receptor. In this review, we summarize considerable research regarding the relationship between HBV and glycosylation as it relates to the development of novel diagnostic tests and therapies for HBV.
Highlights
Hepatitis B virus (HBV) is a well-known pathogenic virus that causes acute/chronic hepatitis in humans
Most patients with chronic hepatitis B acquired the infection via the mother–infant route, called vertical infection, or otherwise horizontal infection such as sexual transmission, drug abuse, and so on, which may involve acute hepatitis caused by a special genotype of HBV
In a review of clinical data, Qiao et al reported that an additional N-glycosylation mutation in the major hydrophilic region of the HBV S gene is a risk indicator for hepatocellular carcinoma (HCC) in patients with chronic hepatitis B [30]
Summary
Hepatitis B virus (HBV) is a well-known pathogenic virus that causes acute/chronic hepatitis in humans. Nucleotide analogue therapy is very effective, most patients require continuous therapy to suppress HBV replication. Previous studies using site-directed mutagenesis of potential N-glycosylation sites have demonstrated the biological significance of Nglycans in HBV envelope proteins [7]. Changes in the glycosylation of HBV envelope proteins and/or hepatocyte proteins could affect the risk of HBV infection. A recent review on glycosylation and virus infection showed the importance of glycans on viral and host proteins in enveloped virus infection [9]. In cases of enveloped viruses, glycans influence the virus replication cycle, the folding/transport of viral glycoproteins, the release of virus, virus transmission, immune escapes, and virulence/pathogenicity of the virus. The biological significance of glycosylation, including glycosylation of specific proteins as biomarkers, is discussed in terms of HBV virology and the current state of glycoscience
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